ArticleBiochemistry2006
Structural analysis of the catalytic core of human telomerase RNA by FRET and molecular modeling.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- RNA folding pathways from all-atom simulations with a variationally improved history-dependent bias.Biophysical journal · 2023Article
- Computer-aided comprehensive explorations of RNA structural polymorphism through complementary simulation methods.QRB discovery · 2022Review
- Review
- Oxoisoaporphines and Aporphines: Versatile Molecules with Anticancer Effects.Molecules (Basel, Switzerland) · 2019Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.RNA (New York, N.Y.) · 2017Article
- Oxoisoaporphine as Potent Telomerase Inhibitor.Molecules (Basel, Switzerland) · 2016Article
- Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: temperature-/urea-dependent folding kinetics and thermodynamics.The journal of physical chemistry. B · 2014Article
- Three-dimensional RNA structure of the major HIV-1 packaging signal region.Structure (London, England : 1993) · 2013Article
- Mapping targetable sites on human telomerase RNA pseudoknot/template domain using 2'-OMe RNA-interacting polynucleotide (RIPtide) microarrays.The Journal of biological chemistry · 2012Article
- Architecture of human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Single-molecule analysis of telomerase structure and function.Current opinion in chemical biology · 2011Review
- Structurally conserved five nucleotide bulge determines the overall topology of the core domain of human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Engineering cis-telomerase RNAs that add telomeric repeats to themselves.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- RNA conformation in catalytically active human telomerase.Journal of the American Chemical Society · 2010Article
- 2-D structure of the A region of Xist RNA and its implication for PRC2 association.PLoS biology · 2010Article
- Solution structure and dynamics of the wild-type pseudoknot of human telomerase RNA.Journal of molecular biology · 2008Article
- Triple-helix structure in telomerase RNA contributes to catalysis.Nature structural & molecular biology · 2008Article
- Single-molecule mechanical unfolding and folding of a pseudoknot in human telomerase RNA.RNA (New York, N.Y.) · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Telomerase is the ribonucleoprotein reverse transcriptase involved in the maintenance of the telomeres, the termini of eukaryotic chromosomes. The RNA component of human telomerase (hTR) consists of 451 nucleotides with the 5' half folding into a highly conserved catalytic core comprising the template region and an adjacent pseudoknot domain (nucleotides 1-208). While the secondary structure of hTR is established, there is little understanding of its three-dimensional (3D) architecture. Here, we have used fluorescence resonance energy transfer (FRET) between fluorescently labelled peptide nucleic acids, hybridized to defined single stranded regions of full length hTR, to evaluate long-range distances. Using molecular modeling, the distance constraints derived by FRET were subsequently used, together with the known secondary structure, to generate a 3D model of the catalytic core of hTR. An overlay of a large set of models generated has provided a low-resolution structure (6.5-8.0 A) that can readily be refined as new structural information becomes available. A notable feature of the modeled structure is the positioning of the template adjacent to the pseudoknot, which brings a number of conserved nucleotides close in space.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.